Inhibition of fibril formation is considered a possible treatment strategy for amyloid-related
diseases. Understanding the molecular nature of inhibitor action is crucial for the design of …

Molecular chaperones are important components in the cellular quality-control machinery
and increasing evidence points to potential new roles for them as suppressors of amyloid …

Protein misfolding can generate toxic intermediates, which underlies several devastating
diseases, such as Alzheimer's disease (AD). The surface of AD-associated amyloid-β …

Attempts to treat Alzheimer's disease with immunotherapy against the β-amyloid (Aβ)
peptide or with enzyme inhibitors to reduce Aβ production have not yet resulted in effective …

The complex kinetics of disease-related amyloid aggregation of proteins such as α-
Synuclein (α-Syn) in Parkinson's disease and Aβ42 in Alzheimer's disease include primary …

Amyloid fibrils—nanoscale fibrillar aggregates with high levels of order—are pathogenic in
some today incurable human diseases; however, there are also many physiologically …

The escalating prevalence of Alzheimer's disease (AD) has prompted extensive research
into potential therapeutic interventions, with a specific focus on molecular targets such as …

Proteins can self-assemble into amyloid fibrils or amorphous aggregates and thereby cause
disease. Molecular chaperones can prevent both these types of protein aggregation, but to …

Amyloid fibrils have been implicated in the pathogenesis of several neurodegenerative
diseases, the most prevalent example being Alzheimer's disease (AD). Despite the …

Background: Aggregated forms of the amyloid-β (Aβ) peptides which form protofibrils and
fibrils in the brain are signatures of Alzheimer's disease (AD). Aggregates are also …